Human recombinant interleukin-1 alpha increases elastase-like enzyme in human uterine cervical fibroblasts.
Production of the elastase-like enzyme, Suc-(Ala)3-p-nitroanilide hydrolase, was examined in human uterine cervical fibroblasts. The metallo-dependent enzyme is present in both media and cellular fractions. Human recombinant interleukin-1 alpha stimulated cells to produce and secrete this elastase-like enzyme. These results suggest that modulation of this enzyme activity by interleukin-1 may play a significant role in the ripening and dilation of the cervix, because elastin is a component of the uterine cervix and its peptides are known to be chemotactic for leukocytes.
Ito
A
A
Department of Biochemistry, Tokyo College of Pharmacy, Japan.
Leppert
P C
PC
Mori
Y
Y
D002478:Cells, Cultured; D002584:Cervix Uteri / Q000201:enzymology*; D005260:Female; D005347:Fibroblasts; D006801:Humans; D066298:In Vitro Techniques; D007375:Interleukin-1 / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000494:pharmacology
D007375:Interleukin-1; D011994:Recombinant Proteins; D010447:Peptide Hydrolases; C023092:succinyltrialanine p-nitroanilide hydrolase